Function and Biology Details
Reaction catalysed:
2 reduced [2Fe-2S] ferredoxin + NAD(+) + H(+) = 2 oxidized [2Fe-2S] ferredoxin + NADH
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- Flavoprotein pyridine nucleotide cytochrome reductase
- 2Fe-2S ferredoxin-type iron-sulfur binding domain
- Ferredoxin-NADP reductase (FNR), nucleotide-binding domain
- Oxidoreductase FAD/NAD(P)-binding
- Flavoprotein pyridine nucleotide cytochrome reductase-like, FAD-binding domain
- Benzoate 1,2-dioxygenase reductase, FAD/NAD binding domain
- Riboflavin synthase-like beta-barrel
- FAD-binding domain, ferredoxin reductase-type
4 more domains
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139754 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Benzoate 1,2-dioxygenase electron transfer component
Molecule details ›
Chains: A, B
Length: 338 amino acids
Theoretical weight: 37.66 KDa
Source organism: Acinetobacter sp.
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 338 amino acids
Theoretical weight: 37.66 KDa
Source organism: Acinetobacter sp.
Expression system: Escherichia coli
UniProt:
- Canonical:
P07771 (Residues: 11-348; Coverage: 97%)
Sequence domains:
- 2Fe-2S iron-sulfur cluster binding domain
- Oxidoreductase FAD-binding domain
- Oxidoreductase NAD-binding domain
